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UBD activates OTUB1. 8 / 8
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"This may help to understand whether phospho-FAT10, while inducing the deubiquitylation of TRAF3, could simultaneously enhance OTUB1 activity in removing K48-ubiquitin chains from RIG-I, thereby impairing its proteasomal degradation.It is interesting to note that the measured IFNβ levels differed always markedly between A549 OTUB1 knockout cells which were treated either with Poly (I:C), or which were infected with IAV (Fig 7E and F)."
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"Further Down the Interferon Induction Cascade: FAT10 Activates the Deubiquitylating Enzyme OTUB1."
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"Importantly, all of these values are up to almost an order of magnitude lower than the K d of each E2 for OTUB1 in the absence of diubiquitin, highlighting the potential for K48 polyubiquitin chains to drive association of OTUB1 with its E2 partners at E2 concentrations on the order of 1 muM or less (XREF_FIG)."
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"The ubiquitin-like modifier FAT10 stimulates OTUB1 deubiquitinase activity in both covalent modification and a noncovalent manner (31)."
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"In summary, from these experiments, we conclude that the FAT10-mediated degradation of TRIM21 results into FAT10-mediated down-regulation of antiviral type-I IFN secretion, though other pathways modulated by FAT10 (OTUB1/TRAF3 axis) also contribute to this down-regulation.Our earlier study had shown that FAT10 KO mice infected with LCMV secreted higher levels of type-I IFNs (Mah et al, 2019)."
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"Moreover, FAT10 was shown to stimulate the stability and the enzymatic activity of OTUB1 in reducing the K63- and K48-linked poly-ubiquitylation of TRAF3 (Bialas et al, 2019), suggesting that FAT10 can alter this pathway at different stages."
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"Remarkably, this effect was abolished in OTUB1 KO cells ( xref and xref ), which strongly suggests that the activation of OTUB1 by phosphorylated FAT10 is responsible for the FAT10-mediated impairment of the antiviral IFN-I response."
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"Phosphorylation modulates the FAT10-mediated activation of OTUB1."
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